The Elongation Cycle

Nierhaus, Knud H.

doi:10.1002/3527603433.ch8

Protein Synthesis and Ribosome Structure 2004

DOI: 10.1002/3527603433.ch8

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The Elongation Cycle

Knud H. Nierhaus

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2006

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Cited by 5 publications

(2 citation statements)

References 106 publications

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“…Finally, the selectivity of a significant number of antibiotics, which inhibits protein synthesis in bacterial but not in eukaryotic systems, is consistent with the large differences between the translation processes in bacterial and eukaryotic cells (16)(17)(18)(19)(20).…”

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confidence: 62%

“…This implies that novel inhibitors directed against these targets are likely to be effective against pathogens which have developed resistance to current inhibitors of protein synthesis. Finally, the selectivity of a significant number of antibiotics, which inhibits protein synthesis in bacterial but not in eukaryotic systems, is consistent with the large differences between the translation processes in bacterial and eukaryotic cells ( − ).…”

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confidence: 57%

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Novel Tetrapeptide Inhibitors of Bacterial Protein Synthesis Produced by a Streptomyces sp.

et al. 2006

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In the course of a microbial product screening aimed at the discovery of novel antibiotics acting on bacterial protein synthesis, a complex of three structurally related tetrapeptides, namely, GE81112 factors A, B, and B1, was isolated from a Streptomyces sp. The screening was based on a cell-free assay of bacterial protein synthesis driven by a model mRNA containing natural initiation signals. In this study we report the production, isolation, and structure determination of these novel, potent and selective inhibitors of cell-free bacterial protein synthesis, which stably bind the 30S ribosomal subunit and inhibit the formation of fMet-puromycin. They did not inhibit translation by yeast ribosomes in vitro. Spectroscopic analyses revealed that they are tetrapeptides constituted by uncommon amino acids. While GE81112 factors A, B, and B1 were effective in inhibiting bacterial protein synthesis in vitro, they were less active against Gram-positive and Gram-negative bacterial cells. Cells grown in minimal medium were more susceptible to the compounds than those grown in rich medium, and this is most likely due to competition or regulation by medium components during peptide uptake. The novelty of the chemical structure and of the specific mode of action on the initiation phase of bacterial protein synthesis makes GE81112 a unique scaffold for designing new drugs.

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confidence: 62%

supporting

confidence: 57%

Novel Tetrapeptide Inhibitors of Bacterial Protein Synthesis Produced by a Streptomyces sp.

et al. 2006

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Non‐Hydrolyzable RNA–Peptide Conjugates: A Powerful Advance in the Synthesis of Mimics for 3′‐Peptidyl tRNA Termini

et al. 2009

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Die Translation kleiner Peptide am Ribosom kann diesem eine Resistenz gegen Macrolidantibiotika verleihen. Zur Aufklärung dieses und ähnlicher Phänomene sind stabile RNA‐Peptid‐Konjugate, die Peptidyl‐tRNA imitieren, wünschenswert, besonders für die strukturbiologische Untersuchung von Ribosomen. Eine flexible Festphasensynthesestrategie macht diese Konjugate nun in effizienter Weise zugänglich, ohne Beschränkungen bezüglich der RNA‐ und Peptidsequenz.

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Non‐Hydrolyzable RNA–Peptide Conjugates: A Powerful Advance in the Synthesis of Mimics for 3′‐Peptidyl tRNA Termini

et al. 2009

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Translation of specific small peptides on the ribosome can confer resistance to macrolide antibiotics. To reveal the molecular details of this and related phenomena, stable RNA-peptide conjugates that mimic peptidyl-tRNA would be desirable, especially for ribosome structural biology. A flexible solid-phase synthesis strategy now allows efficient access to these highly requested derivatives without restriction on the RNA and peptide sequences.

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The Elongation Cycle

Cited by 5 publications

References 106 publications

Novel Tetrapeptide Inhibitors of Bacterial Protein Synthesis Produced by a Streptomyces sp.

Novel Tetrapeptide Inhibitors of Bacterial Protein Synthesis Produced by a Streptomyces sp.

Non‐Hydrolyzable RNA–Peptide Conjugates: A Powerful Advance in the Synthesis of Mimics for 3′‐Peptidyl tRNA Termini

Non‐Hydrolyzable RNA–Peptide Conjugates: A Powerful Advance in the Synthesis of Mimics for 3′‐Peptidyl tRNA Termini

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